Recombinant human VAMP-2 protein

Synaptobrevin 2 (Vehicle-associated membrane, VAMP2), which is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25.

Product Specifications

Product Name Alternative

Vesicle-associated membrane protein 2, VAMP2, SYB2, Synaptobrevin 2, VAMP-2, Synaptobrevin-2, Vesicle-associated membrane protein 2, vesicle-associated membrane protein 2 FLJ11460, RATVAMPB, RATVAMPIR, SYB, VAMP 2, Vesicle associated membrane protein 2, Vesicle-associated membrane protein 2 (synaptobrevin 2) .

Expression System

E.coli

Antigen Species

Human

Tag

His-Tag

Applications

SDS-PAGE

Concentration

1 mg/mL (determined by Bradford assay)

Purity

> 95% by SDS-PAGE

Molecular Weight

13.8 kDa (126aa)

Additionnal Information

VAMP2, vesicle-associated membrane protein 2, VAMP2, SYB2, Synaptobrevin 2, VAMP-2, Synaptobrevin-2, Vesicle-associated membrane protein 2, vesicle-associated membrane protein 2 FLJ11460, RATVAMPB, RATVAMPIR, SYB, VAMP 2, Vesicle associated membrane protein 2, Vesicle-associated membrane protein 2 (synaptobrevin 2) ., VAM0710-10 µg, VAM0710-20 µg, VAM0710-50 µg, VAM0710-100 µg, VAM0710-250 µg, VAM0710-500 µg, VAM0710-1 mg, VAM0710-10, VAM0710-20, VAM0710-50, VAM0710-100, VAM0710-250, VAM0710-500, VAM0710-1

References & Citations

Lin RC. and Scheller RH. (1997) Neuron. 19:1087-1094.; ; Hanson PI. et al (1997) Cell 90:523-535.; ; Scales SJ., et al. (2002) J Biol Chem. 277 (31) :28271-9.; ; Windoffer R et al. (1999) Cell Tissue Res 296:499-510;

Other References

Kalb SR, et al. Functional Characterization of Botulinum Neurotoxin Serotype H as a Hybrid of known Serotypes F and A (BoNT F/A) . (Anal Chem. 2015) {https://pubmed.ncbi.nlm.nih.gov/25731972/}